Purification and Structure of Fucoidanase from Fusarium sp. LD8
Author Information
Author(s): Qianqian Wu, Shuang Ma, Hourong Xiao, Min Zhang, Jingmin Cai
Primary Institution: Hefei University
Hypothesis
The study investigates the purification and structural analysis of fucoidanase isolated from the marine fungus Fusarium sp. LD8.
Conclusion
The purified fucoidanase exhibited a specific activity 22.7 times greater than the crude enzyme, with a molecular weight of approximately 64 kDa and optimal activity at 60°C and pH 6.0.
Supporting Evidence
- The specific activity of the purified fucoidanase was 22.7-fold higher than that of the crude enzyme.
- The enzyme's molecular weight was determined to be about 64 kDa.
- The optimal temperature for fucoidanase activity was found to be 60°C.
- The enzyme showed maximum stability at pH 6.0.
Takeaway
Scientists found a special enzyme from a type of fungus that helps break down a seaweed sugar, and it works best at a warm temperature.
Methodology
Fucoidanase was purified using solid-state fermentation, followed by extraction with citric acid buffer, acetone precipitation, and Sephadex G-100 chromatography.
Digital Object Identifier (DOI)
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